Purification of SOCS (Suppressor of Cytokine Signaling) SH2 Domains for Structural and Functional Studies.

Autor:	Liau NP; The Walter and Eliza Hall Institute of Medical Research, 1G Royal Pde, Parkville, Melbourne, 3052, VIC, Australia.; Department of Medical Biology, University of Melbourne, Royal Pde, Melbourne, 3050, VIC, Australia., Laktyushin A; The Walter and Eliza Hall Institute of Medical Research, 1G Royal Pde, Parkville, Melbourne, 3052, VIC, Australia.; Department of Medical Biology, University of Melbourne, Royal Pde, Melbourne, 3050, VIC, Australia., Babon JJ; The Walter and Eliza Hall Institute of Medical Research, 1G Royal Pde, Parkville, Melbourne, 3052, VIC, Australia. babon@wehi.edu.au.; Department of Medical Biology, University of Melbourne, Royal Pde, Melbourne, 3050, VIC, Australia. babon@wehi.edu.au.
Jazyk:	angličtina
Zdroj:	Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2017; Vol. 1555, pp. 173-182.
DOI:	10.1007/978-1-4939-6762-9_10
Abstrakt:	Src Homology 2 (SH2) domains are protein domains which have a high binding affinity for specific amino acid sequences containing a phosphorylated tyrosine residue. The Suppressors of Cytokine Signaling (SOCS) proteins use an SH2 domain to bind to components of certain cytokine signaling pathways to downregulate the signaling cascade. The recombinantly produced SH2 domains of various SOCS proteins have been used to undertake structural and functional studies elucidating the method of how such targeting occurs. Here, we describe the protocol for the recombinant production and purification of SOCS SH2 domains, with an emphasis on SOCS3.
Databáze:	MEDLINE
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